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Physical and mechanical properties of Albizia procera glulam beam.

ABSTRACT: This research was done to evaluate the feasibility of using Albizia procera for manufacturing glulam beams. The physical and mechanical properties of the A. procera glulam beam were evaluated, and these properties were compared to those of the solid A. procera solid timber. The A. procera glulam beam's physical and mechanical properties were all superior to solid A. procera timber. In comparison to A. procera solid timber, A. procera glulam's density, water absorption (WA), linear expansion (LE), and thickness swelling (TS) all improved by 11.1, 48.4, 44.6, and 37.0%, respectively. Again, compared to A. procera solid timber, the modulus of rupture (MOR) and modulus of elasticity (MOE) of the A. procera glulam beam increased by 27.6 and 29.2%, respectively. Additionally, the ASTM specifications were met by the A. procera glulam beam. As a result, based on the properties, it is possible to make A. procera glulam beams as structural timber products.

SUBMITTER: Das AK

PROVIDER: S-EPMC10382284 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature

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Physical and mechanical properties of Albizia procera glulam beam.

Das Atanu Kumar AK Islam Md Nazrul MN Ghosh Chayan Kumar CK Ghosh Rupak Kumar RK

Heliyon 20230717 8

This research was done to evaluate the feasibility of using Albizia procera for manufacturing glulam beams. The physical and mechanical properties of the A. procera glulam beam were evaluated, and these properties were compared to those of the solid A. procera solid timber. The A. procera glulam beam's physical and mechanical properties were all superior to solid A. procera timber. In comparison to A. procera solid timber, A. procera glulam's dens ...[more]

PMID: 37520963

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Project description:The mechanisms that determine mechanical stabilities of protein folds remain elusive. Our understanding of these mechanisms is vital to both bioengineering efforts and to the better understanding and eventual treatment of pathogenic mutations affecting mechanically important proteins such as titin. We present a new approach to analyze data from single-molecule force spectroscopy for different domains of the giant muscle protein titin. The region of titin found in the I-band of a sarcomere is composed of about 40 Ig-domains and is exposed to force under normal physiological conditions and connects the free-hanging ends of the myosin filaments to the Z-disc. Recent single-molecule force spectroscopy data show a mechanical hierarchy in the I-band domains. Domains near the C-terminus in this region unfold at forces two to three times greater than domains near the beginning of the I-band. Though all of these Ig-domains are thought to share a fold and topology common to members of the Ig-like fold family, the sequences of neighboring domains vary greatly with an average sequence identity of only 25%. We examine in this study the relation of these unique mechanical stabilities of each I-band Ig domain to specific, conserved physical-chemical properties of amino acid sequences in related Ig domains. We find that the sequences of each individual titin Ig domain are very highly conserved, with an average sequence identity of 79% across species that are divergent as humans, chickens, and zebra fish. This indicates that the mechanical properties of each domain are well conserved and tailored to its unique position in the titin molecule. We used the PCPMer software to determine the conservation of amino acid properties in titin Ig domains grouped by unfolding forces into "strong" and "weak" families. We found two motifs unique to each family that may have some role in determining the mechanical properties of these Ig domains. A detailed statistical analysis of properties of individual residues revealed several positions that displayed differentially conserved properties in strong and weak families. In contrast to previous studies, we find evidence that suggests that the mechanical stability of Ig domains is determined by several residues scattered across the beta-sandwich fold, and force sensitive residues are not only confined to the A'-G region.

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Physical and mechanical properties of Albizia procera glulam beam.

Publications

Physical and mechanical properties of <i>Albizia procera</i> glulam beam.

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